| IED ID | IndEnz0018000374 |
| Enzyme Type ID | peroxidase000374 |
| Protein Name |
Basic phospholipase A2 Cc2-PLA2 svPLA2 EC 3.1.1.4 Phosphatidylcholine 2-acylhydrolase |
| Gene Name | |
| Organism | Cerastes cerastes (Horned desert viper) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Viperinae (vipers) Cerastes Cerastes cerastes (Horned desert viper) |
| Enzyme Sequence | NLYQFGKMINHMVGKSPIFSYGDYGCYCGWGGKGTPVDATDRCCFVHDCCYGRANGCDPKLSTYSYNFQNGNIVCGNKYGCLRHICECDRVAAICFGENVNTYDKKFLSSSRCRQTSEQC |
| Enzyme Length | 120 |
| Uniprot Accession Number | P0DPS4 |
| Absorption | |
| Active Site | ACT_SITE 47; /evidence=ECO:0000250|UniProtKB:P14418; ACT_SITE 89; /evidence=ECO:0000250|UniProtKB:P14418 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; |
| DNA Binding | |
| EC Number | 3.1.1.4 |
| Enzyme Function | FUNCTION: Basic phospholipase A2 that inhibits ADP-, thrombin- and arachidonic acid-induced platelet aggregation (PubMed:30239061, PubMed:24384926). It also exhibits anticoagulant effects upon human plasma in vitro (PubMed:30239061). It induces a high hemolytic activity reaching its maximum after 24 hours (PubMed:24384926). It induces a marked elevation of plasmatic levels of interleukin-6 and -10, eosinophil peroxidase and complement lytic activities and it also provokes a drastic increase of lymphocytes, monocytes and neutrophils in peripheral blood accompanied by a rapid intense migration of neutrophils to the peritoneal cavity (PubMed:24384926). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:24384926, ECO:0000269|PubMed:30239061}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (7); Metal binding (4) |
| Keywords | Blood coagulation cascade inhibiting toxin;Calcium;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Hemostasis impairing toxin;Hydrolase;Metal-binding;Platelet aggregation inhibiting toxin;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24384926}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 13,430 |
| Kinetics | |
| Metal Binding | METAL 27; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14418; METAL 29; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14418; METAL 31; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14418; METAL 48; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P14418 |
| Rhea ID | RHEA:15801 |
| Cross Reference Brenda |